Secondary structure prediction for the spectrin 106-amino acid segment, and a proposed model for tertiary structure.
A collective secondary structure prediction for the human erythrocyte spectrin 106-residue repeat segment is developed, based on the sequences of nine segments that have been reported in the literature, utilizing a consensus of several secondary structure prediction methods for locating turn regions. The analysis predicts a five-fold structure, with three alpha-helices and two beta-strand regions, and differs from previous models on the lengths of the helices and the existence of beta-strand structure. We also demonstrate that this structural motif can be folded into tertiary structures that satisfy the experimental spectrin data and several general principles of protein organization.
Xu
Y
Y
Department of Chemistry, Loyola University, Chicago, IL 60626.
Prabhakaran
M
M
Johnson
M E
ME
Fung
L W
LW
D002942:Circular Dichroism; D003198:Computer Simulation; D008958:Models, Molecular; D011487:Protein Conformation; D013049:Spectrin / Q000737:chemistry* / Q000648:ultrastructure; D013237:Stereoisomerism
D013049:Spectrin